Spectral properties of the oxyferrous complex of the heme domain of cytochrome P450BM-3 (CYP102)

Here we describe for the first time the formation of a complex of reduced C YP102 (cytochrome P450 BM-3) heme domain with molecular oxygen. To stabiliz e the oxycomplex, the experiments had to be done under argon atmosphere at cryogenic temperatures (-25 degrees C) in the presence of 50% glycerol. The spectral properties of this species were different from those of another P 450-type autosuffisant enzyme, i.e., the neuronal nitric oxide synthase, On the contrary, the oxyferrous complex of CYP102 possesses spectral properti es similar to those of complexes of microsomal cytochromes P450, e.g., CYP2 B4. (C) 1999 Academic Press.